ID A0A401KNZ1_ASPAW Unreviewed; 1012 AA.
AC A0A401KNZ1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=ATP-dependent DNA helicase CHL1 {ECO:0000256|ARBA:ARBA00017386};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE AltName: Full=ATP-dependent DNA helicase chl1 {ECO:0000256|ARBA:ARBA00016387};
DE AltName: Full=Chromosome loss protein 1 {ECO:0000256|ARBA:ARBA00029709};
GN ORFNames=AAWM_03862 {ECO:0000313|EMBL:GCB20977.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB20977.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB20977.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB20977.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent DNA helicase important for chromosome
CC transmission and normal cell cycle progression in G(2)/M (By
CC similarity). May have a role in changing DNA topology to allow the
CC loading of proteins involved in maintaining sister chromatid cohesion
CC in the vicinity of the centromeres (By similarity). Has a specific role
CC in chromosome segregation during meiosis II.
CC {ECO:0000256|ARBA:ARBA00025396}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 family.
CC {ECO:0000256|ARBA:ARBA00007320, ECO:0000256|RuleBase:RU003888}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB20977.1}.
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DR EMBL; BDHI01000007; GCB20977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KNZ1; -.
DR STRING; 105351.A0A401KNZ1; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProt.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 3.100.10.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR HAMAP; MF_01341; Ribosomal_L15; 1.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR InterPro; IPR030878; Ribosomal_uL15.
DR InterPro; IPR021131; Ribosomal_uL15/eL18.
DR InterPro; IPR036227; Ribosomal_uL15/eL18_sf.
DR InterPro; IPR001196; Ribosomal_uL15_CS.
DR NCBIfam; TIGR00604; rad3; 1.
DR PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR Pfam; PF00828; Ribosomal_L27A; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52080; Ribosomal proteins L15p and L18e; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
DR PROSITE; PS00475; RIBOSOMAL_L15; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:GCB20977.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000286921};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU003888};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU003888}.
FT DOMAIN 4..444
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 103..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 114393 MW; 4DD7CC536917FA16 CRC64;
MELQRNDFHH PYSPYDIQLQ LMRALYSCLE QGKVAVFESP TGTGKSLSLI CGSLTWLRDH
KRSAFQTAVD NATCDDDEPE WMLDFARRES SRMITEKRKE LEERLEKTRK EEEQQRIALE
NPEGPRKKQK YSIPLTESGR LSEDQFTLDD YDSENEEHSK PRGELAHTSE LSPSTLELLE
RFKGQISTAK PGSDDEDNDE VKIFYCSRTH SQLTQFAGEL RRVKMPWSIP KDLLSTDLTG
EEELEERVKH VTLGSRKNLC INPRVSSLEN ATAINERCLD LQQPNVNPQH RCPFLPSKED
ERQVLQFRDH ALSTVKDIED LGKLGKKIGI CPYYASRSVV KDSEVCCLRA RSSIDLVPDE
WQIVTLPYPL LLQRSAREAL NLSVKGHVII IDEAHNLMDA ISNIHSVTVT LSQLQTSLSQ
LTIYGRKFKT RLKGKNRSYV AQVIRLLSSI AAHLRSLLES EKAPEGPVLI SELMSGKGID
QINPYKLSRY LQESKLARKV DGYVEFTRDP SDKQASGSPT VPVLFHIQGF LLSLMNPSAE
GRLFYSKEQG DIQLKYMLLD PTNQFRELVE DARAIILAGG TMSPMTDYMN HLFSYVPASR
LDTFSYGHVI PPENLIAHTL VRGVQGSEFD FTYDARDSEK MIMDLGRTIA TLCHVIPDGV
VAFFPSYDYL GRVLNIWKKP MLGEQGQTVY NLIGQKKPIL SESRDMTVTT EELLQTYANT
VDSGRGALLL SVVGGKLSEG INFSDKLGRG VLIVGLPFPN IRSAVWQAKI QYIEQKTHQQ
ATGSEASRQL AAKAAGRDFY ENSCMRAVNQ CIGRAIRHRN DYAAIVLVDR RYEKPGIQAK
LPAWIKQSLW PHPTTFRPVY QNNKKTDFCV LFLSRGHVSA GYGRIGKHRK HPGGRGMAGG
QHHHRTNLDK YHPGYFGKVG MRYFHKTQQQ FWKPTINLDK LWSLVPAEKR DAYLSGQKTD
TAPVIDLLPL GYSKVLGKGR LPEVPIVVRA RYFSRDAEEK IKAAGGVVEL VA
//